ID KAD1_HUMAN Reviewed; 194 AA. AC P00568; Q9BVK9; Q9UQC7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 3. DT 27-MAR-2024, entry version 228. DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000255|HAMAP-Rule:MF_03171}; DE Short=AK 1 {ECO:0000255|HAMAP-Rule:MF_03171}; DE EC=2.7.4.10 {ECO:0000269|PubMed:2542324}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:2542324}; DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|PubMed:23416111}; DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000255|HAMAP-Rule:MF_03171}; DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_03171}; DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03171}; DE AltName: Full=Myokinase {ECO:0000255|HAMAP-Rule:MF_03171}; GN Name=AK1 {ECO:0000255|HAMAP-Rule:MF_03171}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1. RC TISSUE=Skeletal muscle; RX PubMed=183954; DOI=10.1111/j.1432-1033.1976.tb10787.x; RA von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R.H., RA Pai E.F.; RT "Primary and tertiary structure of the principal human adenylate kinase."; RL Eur. J. Biochem. 68:281-290(1976). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HAAKD TRP-128, CHARACTERIZATION RP OF HAAKD TRP-128, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=2542324; DOI=10.1016/s0021-9258(18)81779-3; RA Matsuura S., Igarashi M., Tanizawa Y., Yamada M., Kishi F., Kajii T., RA Fujii H., Miwa S., Sakurai M., Nakazawa A.; RT "Human adenylate kinase deficiency associated with hemolytic anemia. A RT single base substitution affecting solubility and catalytic activity of the RT cytosolic adenylate kinase."; RL J. Biol. Chem. 264:10148-10155(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RA Noma T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 10-21; 32-44; 64-77; 89-97; 108-128; 156-166 AND RP 172-194, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23416111; DOI=10.1016/j.biocel.2013.02.004; RA Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.; RT "The human adenylate kinase 9 is a nucleoside mono- and diphosphate RT kinase."; RL Int. J. Biochem. Cell Biol. 45:925-931(2013). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG RP AP5A. RG Structural genomics consortium (SGC); RT "Crystal structure of human AK1A in complex with AP5A."; RL Submitted (MAR-2007) to the PDB data bank. RN [12] RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG RP AP4A. RG Structural genomics consortium (SGC); RT "Structure of adenylate kinase 1 in complex with P1, P4- RT di(adenosine)tetraphosphate."; RL Submitted (DEC-2005) to the PDB data bank. RN [13] RP VARIANT HAAKD CYS-164. RX PubMed=9432020; DOI=10.1046/j.1365-2141.1997.4953299.x; RA Qualtieri A., Pedace V., Bisconte M.G., Bria M., Gulino B., Andreoli V., RA Brancati C.; RT "Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G RT substitution at codon 164 of human AK1 gene associated with chronic RT haemolytic anaemia."; RL Br. J. Haematol. 99:770-776(1997). RN [14] RP VARIANTS HAAKD ARG-40; ARG-64 AND ASP-140 DEL. RX PubMed=12649162; DOI=10.1182/blood-2002-07-2288; RA Corrons J.-L., Garcia E., Tusell J.J., Varughese K.I., West C., Beutler E.; RT "Red cell adenylate kinase deficiency: molecular study of 3 new mutations RT (118G>A, 190G>A, and GAC deletion) associated with hereditary RT nonspherocytic hemolytic anemia."; RL Blood 102:353-356(2003). CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate CC group between ATP and AMP (PubMed:2542324). Exhibits nucleoside CC diphosphate kinase activity, catalyzing the production of ATP, CTP, CC GTP, UTP, dATP, dCTP, dGTP and dTTP from the corresponding diphosphate CC substrates with either ATP or GTP as phosphate donor (PubMed:23416111). CC Also catalyzes at a very low rate the synthesis of thiamine CC triphosphate (ThTP) from thiamine diphosphate (ThDP) and ADP (By CC similarity). {ECO:0000250|UniProtKB:P05081, ECO:0000255|HAMAP- CC Rule:MF_03171, ECO:0000269|PubMed:23416111, CC ECO:0000269|PubMed:2542324}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171, CC ECO:0000269|PubMed:2542324}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03171, ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000255|HAMAP-Rule:MF_03171, CC ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'- CC diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, CC ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; CC EC=2.7.4.10; Evidence={ECO:0000269|PubMed:2542324}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate; CC Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P05081}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000269|Ref.11, CC ECO:0000269|Ref.12}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05081}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03171, ECO:0000305|Ref.11, CC ECO:0000305|Ref.12}. CC -!- POLYMORPHISM: This enzyme represents the most common of at least five CC alleles. {ECO:0000305|PubMed:183954}. CC -!- DISEASE: Hemolytic anemia due to adenylate kinase deficiency (HAAKD) CC [MIM:612631]: A disease characterized by hemolytic anemia and CC undetectable erythrocyte adenylate kinase activity. CC {ECO:0000269|PubMed:12649162, ECO:0000269|PubMed:2542324, CC ECO:0000269|PubMed:9432020}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_03171}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Adenylate kinase entry; CC URL="https://en.wikipedia.org/wiki/Adenylate_kinase"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04809; AAA51686.1; -; Genomic_DNA. DR EMBL; AB021871; BAA78534.1; -; mRNA. DR EMBL; BT019580; AAV38387.1; -; mRNA. DR EMBL; BC001116; AAH01116.1; -; mRNA. DR CCDS; CCDS6881.1; -. DR PIR; A33508; KIHUA. DR RefSeq; NP_000467.1; NM_000476.2. DR RefSeq; NP_001305050.1; NM_001318121.1. DR RefSeq; XP_016869916.1; XM_017014427.1. DR RefSeq; XP_016869917.1; XM_017014428.1. DR PDB; 1Z83; X-ray; 1.90 A; A/B/C=1-193. DR PDB; 2C95; X-ray; 1.71 A; A/B=1-193. DR PDB; 7DE3; X-ray; 2.20 A; A=1-194. DR PDB; 7X7S; NMR; -; A=1-194. DR PDBsum; 1Z83; -. DR PDBsum; 2C95; -. DR PDBsum; 7DE3; -. DR PDBsum; 7X7S; -. DR AlphaFoldDB; P00568; -. DR BMRB; P00568; -. DR SMR; P00568; -. DR BioGRID; 106706; 60. DR IntAct; P00568; 25. DR STRING; 9606.ENSP00000223836; -. DR ChEMBL; CHEMBL4925; -. DR DrugBank; DB00640; Adenosine. DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate. DR DrugBank; DB14126; Tenofovir. DR DrugBank; DB09299; Tenofovir alafenamide. DR GlyGen; P00568; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P00568; -. DR MetOSite; P00568; -. DR PhosphoSitePlus; P00568; -. DR SwissPalm; P00568; -. DR BioMuta; AK1; -. DR DMDM; 20178288; -. DR OGP; P00568; -. DR REPRODUCTION-2DPAGE; IPI00018342; -. DR EPD; P00568; -. DR jPOST; P00568; -. DR MassIVE; P00568; -. DR PaxDb; 9606-ENSP00000362271; -. DR PeptideAtlas; P00568; -. DR ProteomicsDB; 51267; -. DR Pumba; P00568; -. DR TopDownProteomics; P00568; -. DR Antibodypedia; 1017; 710 antibodies from 36 providers. DR DNASU; 203; -. DR Ensembl; ENST00000373156.5; ENSP00000362249.1; ENSG00000106992.19. DR Ensembl; ENST00000644144.2; ENSP00000494600.1; ENSG00000106992.19. DR GeneID; 203; -. DR KEGG; hsa:203; -. DR MANE-Select; ENST00000644144.2; ENSP00000494600.1; NM_000476.3; NP_000467.1. DR AGR; HGNC:361; -. DR CTD; 203; -. DR DisGeNET; 203; -. DR GeneCards; AK1; -. DR HGNC; HGNC:361; AK1. DR HPA; ENSG00000106992; Group enriched (choroid plexus, fallopian tube, heart muscle, skeletal muscle, tongue). DR MalaCards; AK1; -. DR MIM; 103000; gene. DR MIM; 612631; phenotype. DR neXtProt; NX_P00568; -. DR OpenTargets; ENSG00000106992; -. DR Orphanet; 86817; Hemolytic anemia due to adenylate kinase deficiency. DR PharmGKB; PA24655; -. DR VEuPathDB; HostDB:ENSG00000106992; -. DR eggNOG; KOG3079; Eukaryota. DR GeneTree; ENSGT00940000158325; -. DR HOGENOM; CLU_032354_0_3_1; -. DR InParanoid; P00568; -. DR OMA; TQCDRMI; -. DR OrthoDB; 1330004at2759; -. DR PhylomeDB; P00568; -. DR TreeFam; TF354283; -. DR BRENDA; 2.7.4.3; 2681. DR PathwayCommons; P00568; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR SABIO-RK; P00568; -. DR SignaLink; P00568; -. DR BioGRID-ORCS; 203; 15 hits in 1191 CRISPR screens. DR EvolutionaryTrace; P00568; -. DR GenomeRNAi; 203; -. DR Pharos; P00568; Tbio. DR PRO; PR:P00568; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P00568; Protein. DR Bgee; ENSG00000106992; Expressed in apex of heart and 100 other cell types or tissues. DR ExpressionAtlas; P00568; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0001520; C:outer dense fiber; IEA:Ensembl. DR GO; GO:0004017; F:adenylate kinase activity; EXP:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:RHEA. DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03171; Adenylate_kinase_AK1; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR028582; AK1. DR InterPro; IPR006267; AK1/5. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR01360; aden_kin_iso1; 1. DR PANTHER; PTHR23359:SF59; ADENYLATE KINASE ISOENZYME 1; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. DR UCD-2DPAGE; P00568; -. DR Genevisible; P00568; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; KW Direct protein sequencing; Disease variant; Hereditary hemolytic anemia; KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Transferase. FT CHAIN 1..194 FT /note="Adenylate kinase isoenzyme 1" FT /id="PRO_0000158910" FT REGION 38..67 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT REGION 131..141 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 18..23 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 39 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 44 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 65..67 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 94..97 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 101 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 132 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 138 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 149 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT BINDING 177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|Ref.11, ECO:0000269|Ref.12" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03171, FT ECO:0000269|PubMed:183954" FT MOD_RES 38 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VARIANT 40 FT /note="G -> R (in HAAKD; dbSNP:rs137853204)" FT /evidence="ECO:0000269|PubMed:12649162" FT /id="VAR_055337" FT VARIANT 64 FT /note="G -> R (in HAAKD; dbSNP:rs137853205)" FT /evidence="ECO:0000269|PubMed:12649162" FT /id="VAR_055338" FT VARIANT 123 FT /note="E -> Q (in dbSNP:rs8192462)" FT /id="VAR_034046" FT VARIANT 128 FT /note="R -> W (in HAAKD; the same mutation in the chicken FT sequence shows reduced adenylate kinase activity; FT dbSNP:rs104894101)" FT /evidence="ECO:0000269|PubMed:2542324" FT /id="VAR_004021" FT VARIANT 140 FT /note="Missing (in HAAKD)" FT /evidence="ECO:0000269|PubMed:12649162" FT /id="VAR_055339" FT VARIANT 164 FT /note="Y -> C (in HAAKD; dbSNP:rs137853203)" FT /evidence="ECO:0000269|PubMed:9432020" FT /id="VAR_055340" FT CONFLICT 9 FT /note="K -> N (in Ref. 5; AAH01116)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="Q -> R (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 181 FT /note="S -> E (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 1..5 FT /evidence="ECO:0007829|PDB:2C95" FT STRAND 10..15 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 21..32 FT /evidence="ECO:0007829|PDB:2C95" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 39..48 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 52..62 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 69..83 FT /evidence="ECO:0007829|PDB:2C95" FT TURN 84..86 FT /evidence="ECO:0007829|PDB:2C95" FT STRAND 90..94 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 99..108 FT /evidence="ECO:0007829|PDB:2C95" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 122..133 FT /evidence="ECO:0007829|PDB:2C95" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 143..156 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 158..167 FT /evidence="ECO:0007829|PDB:2C95" FT STRAND 170..174 FT /evidence="ECO:0007829|PDB:2C95" FT HELIX 179..193 FT /evidence="ECO:0007829|PDB:2C95" SQ SEQUENCE 194 AA; 21635 MW; 95EC5AAA92D1F00F CRC64; MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK //